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Database: UniProt/TrEMBL
Entry: F0ZSP7_DICPU
LinkDB: F0ZSP7_DICPU
Original site: F0ZSP7_DICPU 
ID   F0ZSP7_DICPU            Unreviewed;       519 AA.
AC   F0ZSP7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=DICPUDRAFT_92487 {ECO:0000313|EMBL:EGC33014.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC33014.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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DR   EMBL; GL871162; EGC33014.1; -; Genomic_DNA.
DR   RefSeq; XP_003290441.1; XM_003290393.1.
DR   AlphaFoldDB; F0ZSP7; -.
DR   STRING; 5786.F0ZSP7; -.
DR   EnsemblProtists; EGC33014; EGC33014; DICPUDRAFT_92487.
DR   GeneID; 10504817; -.
DR   KEGG; dpp:DICPUDRAFT_92487; -.
DR   eggNOG; KOG1815; Eukaryota.
DR   InParanoid; F0ZSP7; -.
DR   OMA; HRFCMIC; -.
DR   OrthoDB; 3084186at2759; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0031149; P:sorocarp stalk cell differentiation; IEA:EnsemblProtists.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:EnsemblProtists.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR   CDD; cd22583; Rcat_RBR_ARI7-like; 1.
DR   CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045840; Ariadne.
DR   InterPro; IPR048962; ARIH1-like_UBL.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685:SF461; E3 UBIQUITIN-PROTEIN LIGASE RBRA-RELATED; 1.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF21235; ARI1_UBAl; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 2.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          134..353
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          138..187
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   519 AA;  60235 MW;  89FD5A373F107632 CRC64;
     MTDDEMYEDY DVDDDSAEES GNESLDDENE YDEGTQEFDF DDGQQSQRTH SKLTRQRSFE
     VLNKNDLFSE SHKIIKEVKD VLSIPSDAAV SALLRFMKWN KEKLIERYME NPEKLCSDAG
     VPNVMKLDAP PAKTTVSCLI CLDDYAPDKV FALSCNHKYC LGCWKNYLEI NVGEGPECIY
     TTCPAPKCKV VVHQDAFKAI ISPEIYERYN SFILKSYVDD NPQVKWCPAP GCIYSIRCDR
     KERKEAVLCK CGFQYCFNCN DYDIGDHMPC PCSQVDKWLQ KASDESENVT WMLANTKKCP
     ECRSPIEKNG GCMHMTCRKN AGGCGYEFCW LCRGPWSEHG STTGGYYNCN KYDKSKAKED
     DDKAQDAKTE LEAYMFYYHR YESHRNAMKI ADEQRKNAHL KEQQILSKFD VRSADTKFLM
     EATEQLLRNR RVLQYSYVYG YYLDKKSQER NLFEYLQEDL EKHTNFLSTL YETSLEKLED
     YQGFIKWKEQ VTNYTRITKK FLDNFVEGVA GGLVSTAQH
//
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